ID A0A1R0GVD2_9FUNG Unreviewed; 459 AA.
AC A0A1R0GVD2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
GN ORFNames=AYI68_g5058 {ECO:0000313|EMBL:OLY80841.1};
OS Smittium mucronatum.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133383 {ECO:0000313|EMBL:OLY80841.1, ECO:0000313|Proteomes:UP000187455};
RN [1] {ECO:0000313|EMBL:OLY80841.1, ECO:0000313|Proteomes:UP000187455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALG-7-W6 {ECO:0000313|EMBL:OLY80841.1,
RC ECO:0000313|Proteomes:UP000187455};
RX PubMed=27343289; DOI=10.1093/molbev/msw126;
RA Wang Y., White M.M., Kvist S., Moncalvo J.M.;
RT "Genome-Wide Survey of Gut Fungi (Harpellales) Reveals the First
RT Horizontally Transferred Ubiquitin Gene from a Mosquito Host.";
RL Mol. Biol. Evol. 33:2544-2554(2016).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC {ECO:0000256|RuleBase:RU000325}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000256|ARBA:ARBA00007249,
CC ECO:0000256|RuleBase:RU000325}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLY80841.1}.
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DR EMBL; LSSL01003075; OLY80841.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R0GVD2; -.
DR STRING; 133383.A0A1R0GVD2; -.
DR Proteomes; UP000187455; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01883; EF1_alpha; 1.
DR CDD; cd03693; EF1_alpha_II; 1.
DR CDD; cd03705; EF1_alpha_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR HAMAP; MF_00118_A; EF_Tu_A; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR NCBIfam; TIGR00483; EF-1_alpha; 1.
DR PANTHER; PTHR23115:SF170; ELONGATION FACTOR 1-ALPHA 2; 1.
DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:OLY80841.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000325};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000325};
KW Protein biosynthesis {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:OLY80841.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000187455}.
FT DOMAIN 5..240
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 459 AA; 50102 MW; 799E200E6FF55CC6 CRC64;
MGKEKAHLNV VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEANELG KGSFKYAWVL
DKLKAERERG ITIDITLWKF ETPKYVVTVI DAPGHRDFIK NMITGTSQAD CAILIIAGGI
GEFEAGISKD GQTREHALLA FTLGVRQLIV AVNKMDSNKY SEARFTEITK EVANFIKKVG
FNPKAVPFVP ISGFHGDNMI EQSTNMPWYK GWNKETKSGV SKGFTLLEAI DAVEAPVRPS
DKPLRLPLQD VYKIGGIGTV PVGRVETGII KAGMVVTFAP SNVTTEVKSV EMHHETLTEG
RPGDNVGFNV KNVSVKEIRR GNVCGDSKND PPKETASFVA QVIVLNHPGQ ISNGYTPVLD
CHTAHISCRF AEIIEKMDRR SGKTLEAAPK FIKSGDAAMV KLIPSKPMCV ESFQEYPPLG
RFAVRDMRQT VAVGVIKSVE KTDKSGGKTT KSAAKAAKK
//
